The objective of this research is to study relationships of structure, function, and genetic control of hemoglobins. The work is divided into the following parts: structural determination of new abnormal human hemoglobins; functional studies of new hemoglobins and certain previously reported abnormal hemoglobins with special reference to chemical stability and oxygen binding properties; studies of genetic control of abnormal hemoglobins; determination of amino acid sequences of selected animal hemoglobins; and identification of mechanism and intermediates in the formation of Hb AIc. The abnormal hemoglobins under study are referred to our laboratory by several screening groups with whom we then collaborate in further characterizations. Structural studies will be done by paper peptide mapping and by automatic column chromatography. Oxygen equilibria measurements will be determined by an automatic recording system which simultaneously measures oxygen partial pressure and fractional saturation of hemoglobin. Correlations of the structure, function, and genetic data are being attempted in order to better understand this model protein system. BIBLIOGRAPHIC REFERENCES: R.T. Jones and R.D. Koler. A Proposal for Reporting and Recording of Studies of Abnormal Human Hemoglobins. In: Preceedings of the ICSH Expert Panel on Abnormal Haemoglobins and Thalassaemia. R.M. Schmidt (Ed.), Academic Press (1975). pp 311-322. G.H. Bare, P.A. Bromberg, J.O. Alben, B. Brimhall, R.T. Jones, S. Mintz and I. Rother. Altered C-terminal Salt Bridges in Haemoglobin York Cause High Oxygen Affinity. Nature 259: 155-156 (1976).